BMRB Entry 30170

Name: TIRAP phosphoinositide-binding motif
Published: 2017-03-02

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PDB ID: 5t7q
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30170
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

TIRAP phosphoinositide-binding motif

Deposition date:

2016-09-05

Original release date:

2017-03-02

Authors:

Capelluto, D.; Ellena, J.; Armstrong, G.; Zhao, X.; Xiao, S.

Citation:

Citation: Zhao, X.; Xiong, W.; Xiao, S.; Ellena, J.; Armstrong, G.; Finkielstein, C.; Capelluto, D.. "Membrane targeting of TIRAP is negatively regulated by phosphorylation in its phosphoinositide-binding motif" Sci. Rep. 7, 43043-43043 (2017).
PubMed: 28225045

Assembly members:

Assembly members:
entity_1, polymer, 21 residues, 2550.200 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KKPLGKMADWFRQTLLKKPK K

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	61
15N chemical shifts	19
1H chemical shifts	19

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 21 residues - 2550.200 Da.

1

LYS

PRO

LEU

GLY

LYS

MET

ALA

ASP

TRP

2

PHE

ARG

GLN

THR

LEU

LYS

PRO

LYS

3

LYS

Samples:

sample_1: TIRAP PBM, [U-99% 13C; U-99% 15N], 0.4 ± 0.04 mM

sample_conditions_1: ionic strength: 60 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D TOCSYHSQC	sample_1	isotropic	sample_conditions_1
3D NOESYHSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CS-Rosetta v3.5, Shen, Vernon, Baker and Bax - refinement, structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AvanceIII 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks